Recombinant Human BBS7 Protein, N-His

Reference: YHK78001
Product nameRecombinant Human BBS7 Protein, N-His
Origin speciesHuman
Expression systemProkaryotic expression
Molecular weight27.32 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeGly380-Glu599
Aliases /SynonymsBardet-Biedl syndrome 7 protein, BBS2-like protein 1, BBS7, BBS2L1
ReferenceYHK78001
NoteFor research use only.

Description of Recombinant Human BBS7 Protein, N-His

Introduction

Recombinant Human BBS7 Protein is a type of protein that is produced using recombinant DNA technology. It is a member of the Bardet-Biedl syndrome (BBS) protein family and plays a crucial role in the development and maintenance of cilia, which are hair-like structures found on the surface of cells. This protein is essential for various cellular processes and has been extensively studied for its structure, activity, and potential applications.

Structure of Recombinant Human BBS7 Protein

The human BBS7 gene is located on chromosome 4 and encodes for a protein with a molecular weight of approximately 73 kDa. The recombinant form of this protein is produced by cloning the BBS7 gene into an expression vector and then expressing it in a suitable host cell. The resulting protein has the same amino acid sequence as the native BBS7 protein and is therefore identical in structure.

The BBS7 protein has a conserved coiled-coil domain, which is important for protein-protein interactions. It also contains a BBSome complex subunit 7 (BBS7) domain, which is essential for its function in cilia formation and maintenance. Furthermore, the BBS7 protein has been shown to interact with other BBS proteins, forming a complex that is crucial for cilia function.

Activity of Recombinant Human BBS7 Protein

The primary function of BBS7 protein is to regulate the assembly and maintenance of cilia. Cilia are microtubule-based organelles that extend from the surface of cells and play important roles in cell signaling, sensory perception, and motility. BBS7 is involved in the formation of the BBSome complex, which is responsible for transporting proteins to the cilia and regulating their function.

Studies have also shown that BBS7 protein is involved in the regulation of various signaling pathways, including the Wnt and Hedgehog pathways. It has been suggested that BBS7 may act as a negative regulator of these pathways, which are important for embryonic development and tissue homeostasis.

Applications of Recombinant Human BBS7 Protein

Recombinant Human BBS7 Protein has a wide range of potential applications in both research and therapeutic settings. Its role in cilia formation and maintenance makes it an important target for studying ciliopathies, which are a group of genetic disorders caused by defects in cilia function. Mutations in the BBS7 gene have been linked to Bardet-Biedl syndrome, a rare disorder characterized by obesity, retinal degeneration, and kidney dysfunction. Therefore, recombinant BBS7 protein can be used to study the underlying mechanisms of this disorder and potentially develop new treatments.

Additionally, BBS7 protein has been shown to interact with other proteins involved in cellular signaling pathways, making it a potential target for drug development. Modulating the activity of BBS7 may have therapeutic benefits for conditions such as cancer, where these signaling pathways are often dysregulated.

In conclusion, Recombinant Human BBS7 Protein is a crucial protein involved in cilia formation, cellular signaling, and potential therapeutic applications. Its well-defined structure and activity make it a valuable tool for studying ciliopathies and developing new treatments for various diseases. Further research on this protein will undoubtedly uncover more insights into its function and potential applications.

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